ID J3HY91_9BRAD Unreviewed; 1105 AA.
AC J3HY91;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:EJN09268.1};
GN ORFNames=PMI42_06841 {ECO:0000313|EMBL:EJN09268.1};
OS Bradyrhizobium sp. YR681.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1144344 {ECO:0000313|EMBL:EJN09268.1, ECO:0000313|Proteomes:UP000007272};
RN [1] {ECO:0000313|EMBL:EJN09268.1, ECO:0000313|Proteomes:UP000007272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR681 {ECO:0000313|EMBL:EJN09268.1,
RC ECO:0000313|Proteomes:UP000007272};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJN09268.1}.
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DR EMBL; AKIY01000285; EJN09268.1; -; Genomic_DNA.
DR RefSeq; WP_008142012.1; NZ_AKIY01000285.1.
DR AlphaFoldDB; J3HY91; -.
DR PATRIC; fig|1144344.3.peg.6217; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000007272; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 3..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 776..877
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 1022..1105
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 1105 AA; 120371 MW; 53E7423199E3D804 CRC64;
MSEQEKPGFC TLCRSRCGTI NVVENDRLIA VRPNPAHPTG KALCPKGRAA PEIAHSARRL
KTPLRRTAPK GAADPGFVPI SWDEALGEIA ERLGRYREET GPESVAFAVT SGSSSSTSDS
LDWIQRFIRG FGSPNNCFST EICNWHKDHA HAFTFGCGLP TADYRNSELI LLWGHNPANV
WLAQAEAISA AQARGARLAV IDPRRTGSAR DADLWLRIRP GTDAALALGL ARWLIVNRAY
DAKFVRHWTN AAFLVRNSDG CFLRAGDVGL EGDGFLVWDE AAGRAVLAED GLAAAALEGS
FDIAGLDGPI ACRTGFDHYV AAAEPYDPAT VERITGIPAA QVEQLAATIA AAASVCYHGW
TGLGQHTNAS QTERAVATLY ALTGCFDAPG GNVRMPSLPV PALHSMAMIA PETRARTLGL
SQRPLGPPTD GWITSSDFYD AALTGKPYRV RALFAFGSNL LVSHPAPERG REALKALDFQ
VHCDPFLNPT AEMADIVLPV SSPWEHEALR LGFEISPEAQ ELVQLRPQMI PRQGEARSDM
WIVFQLAKRL GMGELFFDGD VEKGFEHLLA PLGLDLEALR AKPEGIRVPL AHVHRKYETT
GFATQTGKAE LYSELLHRHG YPAVPRFIEP AERRDEAFPL TLFSANNGYF CHSQHRGINA
LRRKRAEPTA EIHPELARRR HIEEGDWMRV RSRTGAIRMR AAFNDALAQD VVASDYGWWQ
PAPDLGLPGY LPDETQPVGA SFNAVIAENG RDPLSGALAL RSFACDVAPE ESTSWQGWRS
FAVAERREEC SDVVALTLRP VDGGSLPAFR PGQYVSVRIG EAIRSYSLTG AAVVSPEAYA
IGVRHIEGGQ VSTAIRHALA PGDVVELQPP KGGFVLPRRN EFPVVLIAGG IGITPFLSYL
ETLEGAADEP RVMLHYGCRD GQSRPFQHRL EALRQRLPNL TLVTHLSRPR SGDRFDRQGR
FTVSDIDPEL LHKRARFYMC ASDAMMDEVS AGLQARGVPA FEIFRERFRS PAPPALDGLV
PRQIHFARSG RTLTWSPQVP LTSILAAAEG AGLTLPSGCR VGQCESCAVP MKSGEIRHLV
DCADLDEGQC LTCQAVPLSD LVIDA
//
